ID UBC2_CANAL Reviewed; 179 AA. AC O74201; A0A1D8PRG3; Q5A0A0; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 27-MAR-2024, entry version 150. DE RecName: Full=Ubiquitin-conjugating enzyme E2 2; DE EC=2.3.2.23; DE AltName: Full=E2 ubiquitin-conjugating enzyme 2; DE AltName: Full=Radiation sensitivity protein 6; DE AltName: Full=Ubiquitin carrier protein UBC2; DE AltName: Full=Ubiquitin-protein ligase UBC2; GN Name=UBC2; Synonyms=RAD6; OrderedLocusNames=CAALFM_C703870WA; GN ORFNames=CaO19.7195; OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=237561; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=3153A; RA Leng P., Brown A.J.P.; RT "Molecular cloning and characterisation of CaRAD6 gene from Candida RT albicans."; RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION. RC STRAIN=3153A; RX PubMed=10712706; DOI=10.1046/j.1365-2958.2000.01801.x; RA Leng P., Sudbery P.E., Brown A.J.P.; RT "Rad6p represses yeast-hypha morphogenesis in the human fungal pathogen RT Candida albicans."; RL Mol. Microbiol. 35:1264-1275(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=15123810; DOI=10.1073/pnas.0401648101; RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., RA Scherer S.; RT "The diploid genome sequence of Candida albicans."; RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004). RN [4] RP GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52; RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D., RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M., RA Chibana H., Nantel A., Magee P.T.; RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned RT on the eight chromosomes."; RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97; RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.; RT "Assembly of a phased diploid Candida albicans genome facilitates allele- RT specific measurements and provides a simple model for repeat and indel RT structure."; RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013). CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other CC proteins. Plays a role in transcription regulation by catalyzing the CC monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives CC a specific tag for epigenetic transcriptional activation and is also a CC prerequisite for H3K4me and H3K79me formation. Also involved in CC postreplication repair of UV-damaged DNA, in N-end rule-dependent CC protein degradation and in sporulation. {ECO:0000255|PROSITE- CC ProRule:PRU00388, ECO:0000269|PubMed:10712706}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin- CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin- CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE- CC ProRule:PRU10133}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000255|PROSITE-ProRule:PRU00388}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5VVX9}. Nucleus CC {ECO:0000250|UniProtKB:Q5VVX9}. CC -!- INDUCTION: Up-regulated by UV radiation, heat shock, osmotic stress and CC nitrogen starvation. {ECO:0000269|PubMed:10712706}. CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. CC {ECO:0000255|PROSITE-ProRule:PRU00388}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF036707; AAC24765.1; -; mRNA. DR EMBL; AF118145; AAD45241.1; -; Genomic_DNA. DR EMBL; CP017629; AOW30727.1; -; Genomic_DNA. DR RefSeq; XP_019331041.1; XM_019475496.1. DR AlphaFoldDB; O74201; -. DR SMR; O74201; -. DR STRING; 237561.O74201; -. DR EnsemblFungi; C7_03870W_A-T; C7_03870W_A-T-p1; C7_03870W_A. DR GeneID; 3643143; -. DR KEGG; cal:CAALFM_C703870WA; -. DR CGD; CAL0000194082; RAD6. DR VEuPathDB; FungiDB:C7_03870W_A; -. DR eggNOG; KOG0419; Eukaryota. DR HOGENOM; CLU_030988_10_3_1; -. DR InParanoid; O74201; -. DR OMA; DHKSQYI; -. DR OrthoDB; 5478564at2759; -. DR UniPathway; UPA00143; -. DR Proteomes; UP000000559; Chromosome 7. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD. DR GO; GO:0033503; C:HULC complex; IBA:GO_Central. DR GO; GO:1990304; C:MUB1-RAD6-UBR2 ubiquitin ligase complex; IEA:EnsemblFungi. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0097505; C:Rad6-Rad18 complex; IEA:EnsemblFungi. DR GO; GO:1990305; C:RAD6-UBR2 ubiquitin ligase complex; IEA:EnsemblFungi. DR GO; GO:1990303; C:UBR1-RAD6 ubiquitin ligase complex; IEA:EnsemblFungi. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0070628; F:proteasome binding; IEA:EnsemblFungi. DR GO; GO:0003697; F:single-stranded DNA binding; IEA:EnsemblFungi. DR GO; GO:0017116; F:single-stranded DNA helicase activity; IEA:EnsemblFungi. DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IGI:CGD. DR GO; GO:0034644; P:cellular response to UV; IMP:CGD. DR GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IEA:EnsemblFungi. DR GO; GO:0006974; P:DNA damage response; IEP:CGD. DR GO; GO:0006281; P:DNA repair; IBA:GO_Central. DR GO; GO:0006353; P:DNA-templated transcription termination; IEA:EnsemblFungi. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:EnsemblFungi. DR GO; GO:0042275; P:error-free postreplication DNA repair; IEA:EnsemblFungi. DR GO; GO:0070987; P:error-free translesion synthesis; IEA:EnsemblFungi. DR GO; GO:0042276; P:error-prone translesion synthesis; IEA:EnsemblFungi. DR GO; GO:0030447; P:filamentous growth; IMP:CGD. DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IEA:EnsemblFungi. DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IEA:EnsemblFungi. DR GO; GO:2000639; P:negative regulation of SREBP signaling pathway; IEA:EnsemblFungi. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central. DR GO; GO:0090089; P:regulation of dipeptide transport; IEA:EnsemblFungi. DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW. DR GO; GO:0120174; P:stress-induced homeostatically regulated protein degradation pathway; IEA:EnsemblFungi. DR GO; GO:0031509; P:subtelomeric heterochromatin formation; IEA:EnsemblFungi. DR GO; GO:0000722; P:telomere maintenance via recombination; IEA:EnsemblFungi. DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:EnsemblFungi. DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:EnsemblFungi. DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:EnsemblFungi. DR CDD; cd00195; UBCc; 1. DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1. DR InterPro; IPR000608; UBQ-conjugat_E2. DR InterPro; IPR023313; UBQ-conjugating_AS. DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD. DR PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1. DR PANTHER; PTHR24067:SF254; UBIQUITIN-CONJUGATING ENZYME E2-17 KDA; 1. DR Pfam; PF00179; UQ_con; 1. DR SMART; SM00212; UBCc; 1. DR SUPFAM; SSF54495; UBC-like; 1. DR PROSITE; PS00183; UBC_1; 1. DR PROSITE; PS50127; UBC_2; 1. PE 2: Evidence at transcript level; KW ATP-binding; Chromatin regulator; Cytoplasm; DNA damage; DNA repair; KW Nucleotide-binding; Nucleus; Reference proteome; Sporulation; KW Transcription; Transcription regulation; Transferase; KW Ubl conjugation pathway. FT CHAIN 1..179 FT /note="Ubiquitin-conjugating enzyme E2 2" FT /id="PRO_0000082528" FT DOMAIN 4..150 FT /note="UBC core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388" FT REGION 1..28 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 145..179 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 151..179 FT /note="Acidic tail" FT COMPBIAS 148..179 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 88 FT /note="Glycyl thioester intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388, FT ECO:0000255|PROSITE-ProRule:PRU10133" SQ SEQUENCE 179 AA; 20576 MW; 24A081B5F8E4D316 CRC64; MSTPARRRLM RDFKRMQQDP PSGVSASPLP DNVMKWNAVI IGPSDTPFED GTFRLLLSFD EQYPNKPPQV KFISEMFHPN VYASGELCLD ILQNRWSPTY DVSSILTSVQ SLLNDPNISS PANVEAANLY KDHRSLYVKR VRETVENSWN DDDDEEEEEE DEDEAEDEDD DDDDNIDED //